Disruption of Ebola NP0VP35 Inclusion Body-like Structures reduce Viral Infection

Chao Wu, Nicole D. Wagner, Austin B. Moyle, Annie Feng, Nitin Sharma, Sarah H. Stubbs, Callie Donahue, Robert A. Davey, Michael L. Gross, Daisy W. Leung, Gaya K. Amarasinghe

Research output: Contribution to journalArticlepeer-review


Viral inclusion bodies (IBs) are potential sites of viral replication and assembly. How viral IBs form remains poorly defined. Here we describe a combined biophysical and cellular approach to identify the components necessary for IB formation during Ebola virus (EBOV) infection. We find that the eNP0VP35 complex containing Ebola nucleoprotein (eNP) and viral protein 35 (eVP35), the functional equivalents of nucleoprotein (N) and phosphoprotein (P) in non-segmented negative strand viruses (NNSVs), phase separates to form inclusion bodies. Phase separation of eNP0VP35 is reversible and modulated by ionic strength. The multivalency of eVP35, and not eNP, is also critical for phase separation. Furthermore, overexpression of an eVP35 peptide disrupts eNP0VP35 complex formation, leading to reduced frequency of IB formation and limited viral infection. Together, our results show that upon EBOV infection, the eNP0VP35 complex forms the minimum unit to drive IB formation and viral replication.

Original languageEnglish
Article number168241
JournalJournal of Molecular Biology
Issue number20
StatePublished - Oct 15 2023


  • biomolecular condensate
  • Ebola
  • inclusion body
  • phase separation
  • viral replication organelle


Dive into the research topics of 'Disruption of Ebola NP0VP35 Inclusion Body-like Structures reduce Viral Infection'. Together they form a unique fingerprint.

Cite this